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O4878

Sigma-Aldrich

Oxaloacetate Decarboxylase from Pseudomonas sp.

lyophilized powder, ≥100 units/mg solid

Synonym(s):

OAD

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

≥100 units/mg solid

storage temp.

−20°C

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General description

Oxaloacetate decarboxylase or OAD functions as a Na pump in anaerobic bacteria. It is a membrane protein consisting of three subunits, α, β and γ with the α subunit containing the carboxylase activity.

Application

Oxaloacetate Decarboxylase from Pseudomonas sp. has been used in the digestion of the low molecular weight (LMW) human milk fraction (5kF fraction) and as a positive control for deciphering C. thermocellum oxaloacetate decarboxylase activity.
Oxaloacetate decarboxylase has been used in a study to assess turnover and accessibility of a reentrant loop of the Na(+)-glutamate transporter GltS. It has also been used in a study to investigate fermentation and metabolic characteristics of Gluconacetobacter oboediens for different carbon sources.

Biochem/physiol Actions

Oxaloacetate Decarboxylase catalyzes the decarboxylation of oxaloacetate and requires manganese and magnesium for its activity. It is associated with a wide vareity of Gram-negative bacteria.

Unit Definition

One unit will convert 1.0 μmole of oxalacetate to pyruvate and CO2 per min at pH 8.0 at 25 °C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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N E Labrou et al.
Archives of biochemistry and biophysics, 365(1), 17-24 (1999-05-01)
Oxaloacetate decarboxylase (OXAD), the enzyme that catalyzes the decarboxylation of oxaloacetate to pyruvic acid and carbon dioxide, was purified 245-fold to homogeneity from Pseudomonas stutzeri. The three-step purification procedure comprised anion-exchange chromatography, metal-chelate affinity chromatography, and biomimetic-dye affinity chromatography. Estimates
Determining citrate in fruit juices using a biosensor with citrate lyase and oxaloacetate decarboxylase in a flow injection analysis system.
Kim, M.
Food Chemistry, 99(4), 851-857 (2006)
Oxaloacetate Decarboxylase fromPseudomonas stutzeri: Purification and Characterization
Labrou NE and Clonis YD
Archives of Biochemistry and Biophysics, 365(1), 17-24 (1999)
Pius Dahinden et al.
Archives of microbiology, 182(5), 414-420 (2004-10-19)
Archaeoglobus fulgidus harbors three consecutive and one distantly located gene with similarity to the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae (KpOadGAB). The water-soluble carboxyl transferase (AfOadA) and the biotin protein (AfOadC) were readily synthesized in Escherichia coli, but the
Pius Dahinden et al.
Archives of microbiology, 183(2), 121-129 (2005-01-14)
The oxaloacetate decarboxylase (OAD) Na(+) pump consists of subunits alpha, beta, and gamma, which are expressed from an oadGAB gene cluster present in various anaerobic bacteria. Vibrio cholerae has two copies of oad genes, which are termed oad-1 and oad-2.

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